Influenza Hemagglutinin and Neuraminidase Membrane Glycoproteins*
Identifieur interne : 000933 ( Pmc/Checkpoint ); précédent : 000932; suivant : 000934Influenza Hemagglutinin and Neuraminidase Membrane Glycoproteins*
Auteurs : Steven J. Gamblin [Royaume-Uni] ; John J. Skehel [Royaume-Uni]Source :
- The Journal of Biological Chemistry [ 0021-9258 ] ; 2010.
Abstract
Considerable progress has been made toward understanding the structural basis of the interaction of the two major surface glycoproteins of influenza A virus with their common ligand/substrate: carbohydrate chains terminating in sialic acid. The specificity of virus attachment to target cells is mediated by hemagglutinin, which acquires characteristic changes in its receptor-binding site to switch its host from avian species to humans. Anti-influenza drugs mimic the natural sialic acid substrate of the virus neuraminidase enzyme but utilize the much tighter binding of the drugs for efficacy. Resistance to one of the two main antiviral drugs is differentially acquired by the two distinct subsets of neuraminidase as a consequence of structural differences in the enzyme active site between the two phylogenetic groups.
Url:
DOI: 10.1074/jbc.R110.129809
PubMed: 20538598
PubMed Central: 2937864
Affiliations:
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PMC:2937864Le document en format XML
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<front><div type="abstract" xml:lang="en"><p>Considerable progress has been made toward understanding the structural basis of the interaction of the two major surface glycoproteins of influenza A virus with their common ligand/substrate: carbohydrate chains terminating in sialic acid. The specificity of virus attachment to target cells is mediated by hemagglutinin, which acquires characteristic changes in its receptor-binding site to switch its host from avian species to humans. Anti-influenza drugs mimic the natural sialic acid substrate of the virus neuraminidase enzyme but utilize the much tighter binding of the drugs for efficacy. Resistance to one of the two main antiviral drugs is differentially acquired by the two distinct subsets of neuraminidase as a consequence of structural differences in the enzyme active site between the two phylogenetic groups.</p>
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</TEI>
<pmc article-type="review-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Biol Chem</journal-id>
<journal-id journal-id-type="hwp">jbc</journal-id>
<journal-id journal-id-type="pmc">jbc</journal-id>
<journal-id journal-id-type="publisher-id">JBC</journal-id>
<journal-title-group><journal-title>The Journal of Biological Chemistry</journal-title>
</journal-title-group>
<issn pub-type="ppub">0021-9258</issn>
<issn pub-type="epub">1083-351X</issn>
<publisher><publisher-name>American Society for Biochemistry and Molecular Biology</publisher-name>
<publisher-loc>9650 Rockville Pike, Bethesda, MD 20814, U.S.A.</publisher-loc>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">20538598</article-id>
<article-id pub-id-type="pmc">2937864</article-id>
<article-id pub-id-type="publisher-id">R110.129809</article-id>
<article-id pub-id-type="doi">10.1074/jbc.R110.129809</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Minireviews</subject>
</subj-group>
<subj-group><subject>Glycobiology and Extracellular Matrices</subject>
</subj-group>
</article-categories>
<title-group><article-title>Influenza Hemagglutinin and Neuraminidase Membrane Glycoproteins<xref ref-type="fn" rid="FN1">*</xref>
</article-title>
<alt-title alt-title-type="short">MINIREVIEW: Influenza HA and NA Membrane Glycoproteins</alt-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Gamblin</surname>
<given-names>Steven J.</given-names>
</name>
<xref ref-type="aff" rid="aff1"></xref>
<xref ref-type="corresp" rid="cor1"><sup>1</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Skehel</surname>
<given-names>John J.</given-names>
</name>
<xref ref-type="aff" rid="aff1"></xref>
<xref ref-type="corresp" rid="cor2"><sup>2</sup>
</xref>
</contrib>
<aff id="aff1">From the Medical Research Council National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, United Kingdom</aff>
</contrib-group>
<author-notes><corresp id="cor1"><label>1</label>
To whom correspondence may be addressed. E-mail: <email>sgambli@nimr.mrc.ac.uk</email>
.</corresp>
<corresp id="cor2"><label>2</label>
To whom correspondence may be addressed. E-mail: <email>skeheljj@nimr.mrc.ac.uk</email>
.</corresp>
</author-notes>
<pub-date pub-type="ppub"><day>10</day>
<month>9</month>
<year>2010</year>
</pub-date>
<pub-date pub-type="epub"><day>10</day>
<month>6</month>
<year>2010</year>
</pub-date>
<pub-date pub-type="pmc-release"><day>10</day>
<month>6</month>
<year>2010</year>
</pub-date>
<pmc-comment> PMC Release delay is 0 months and 0 days and was based on the
. </pmc-comment>
<volume>285</volume>
<issue>37</issue>
<fpage>28403</fpage>
<lpage>28409</lpage>
<permissions><copyright-statement>© 2010 by The American Society for Biochemistry and Molecular Biology, Inc.</copyright-statement>
<license license-type="open-access"><license-p><italic>Author's Choice</italic>
—Final version full access.</license-p>
<license-p><ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by-nc/3.0/">Creative Commons Attribution Non-Commercial License</ext-link>
applies to Author Choice Articles</license-p>
</license>
</permissions>
<self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zbc03710028403.pdf"></self-uri>
<abstract><p>Considerable progress has been made toward understanding the structural basis of the interaction of the two major surface glycoproteins of influenza A virus with their common ligand/substrate: carbohydrate chains terminating in sialic acid. The specificity of virus attachment to target cells is mediated by hemagglutinin, which acquires characteristic changes in its receptor-binding site to switch its host from avian species to humans. Anti-influenza drugs mimic the natural sialic acid substrate of the virus neuraminidase enzyme but utilize the much tighter binding of the drugs for efficacy. Resistance to one of the two main antiviral drugs is differentially acquired by the two distinct subsets of neuraminidase as a consequence of structural differences in the enzyme active site between the two phylogenetic groups.</p>
</abstract>
<kwd-group><kwd>Viral Immunology</kwd>
<kwd>Viral Protein</kwd>
<kwd>Virus Assembly</kwd>
<kwd>Virus Entry</kwd>
<kwd>Virus Structure</kwd>
<kwd>Virus</kwd>
</kwd-group>
</article-meta>
</front>
</pmc>
<affiliations><list><country><li>Royaume-Uni</li>
</country>
</list>
<tree><country name="Royaume-Uni"><noRegion><name sortKey="Gamblin, Steven J" sort="Gamblin, Steven J" uniqKey="Gamblin S" first="Steven J." last="Gamblin">Steven J. Gamblin</name>
</noRegion>
<name sortKey="Skehel, John J" sort="Skehel, John J" uniqKey="Skehel J" first="John J." last="Skehel">John J. Skehel</name>
</country>
</tree>
</affiliations>
</record>
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